ID B0XDW1_CULQU Unreviewed; 1464 AA.
AC B0XDW1;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN Name=6051386 {ECO:0000313|EnsemblMetazoa:CPIJ017308-PA};
GN ORFNames=CpipJ_CPIJ017308 {ECO:0000313|EMBL:EDS45668.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS45668.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS45668.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ017308-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ017308-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001593};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS232786; EDS45668.1; -; Genomic_DNA.
DR RefSeq; XP_001867833.1; XM_001867798.1.
DR STRING; 7176.B0XDW1; -.
DR EnsemblMetazoa; CPIJ017308-RA; CPIJ017308-PA; CPIJ017308.
DR KEGG; cqu:CpipJ_CPIJ017308; -.
DR VEuPathDB; VectorBase:CPIJ017308; -.
DR VEuPathDB; VectorBase:CQUJHB008051; -.
DR eggNOG; KOG3618; Eukaryota.
DR HOGENOM; CLU_001072_12_0_1; -.
DR InParanoid; B0XDW1; -.
DR OMA; FTAMPPG; -.
DR OrthoDB; 3686360at2759; -.
DR Proteomes; UP000002320; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009975; F:cyclase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016849; F:phosphorus-oxygen lyase activity; IEA:InterPro.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 2.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF8; ADENYLATE CYCLASE TYPE 9; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 108..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 992..1012
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1018..1039
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1073..1096
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1108..1127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1134..1152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1189..1206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 374..501
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 1267..1404
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 566..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1464 AA; 163595 MW; D4784BF3235A0627 CRC64;
MLEAAKICRR VPGSTSNHRR STSFTTMPPV LTDSQKGSVE DIQISLAPYI QSYLTQTGRR
PSCCSVMLPV AFERAAPRSW FDPRFDSPVL EGQFQSSVFP QIRLKFRFAL FYILLCSLVW
LFYFLFDGGP TQYTLLTVSI GLILVFGLVG MWLTHTDVYR AHTNLISSTC AILLCLFSLF
LLLFTDEALS PLGHFSICIE VVMLIYTIIP LPLWLCCTIT TVYSVCFEVL SFFCQLHYDQ
QPSVESLGQG PDRFDGDSTG NFVYKIVTIR VLIQLCVHIL GVHILIMTVV RMRGTFMKVG
QNLLVRRQLE MEKQLKEKMI HSMMPPKVAD LLLKESGSVV KGMSFDQCPP RRATPSDLKS
LFRPFHMNSM DNVSILFADI VGFTKMSSTK TAEQLVEILN DLFERFDDLC LMNGCEKIST
LGDCYYCVSG CPEPRPDHAI CCVEMGLGMI QSIRVFDAQR QEGVKMRVGV HTGTVLCGIV
GTKRVKFDVW SNDVTLANRM ESSGRPDQVH VSEETCSFLG DSYFIEEGEE VDGHRTYFVL
GKKQDLVSSI TEGLSSIGLP PGDHLLLSSS PLDTSSGGGA AHPHHPHAHH HHSFSQSATN
LSSIIRPFLR HPPPARPRPR IASLSKMTKF LKGKSSASHN NHHVVTANGG LDKPKIIVST
KSMPNGIDSD EEGGEAVAVS SVINEKSSGG FRSWKVGKFL KRMDSGGTAD AVGTDKQDCD
RRGEVEVPCL GEVQREGCSS GVYQQLPIVI VTPRPSCHTL EGADLFVPGE WRQSRSDISP
FARTGSYRSQ QCEKASLVTE APVGGRGVRR SRRIVWRLEV GVGMGRKDSG IRSNSRRSSI
QQHIMLMNQS AALSAHRVSG YFTSSQSSLS AVVAASGMNA ADGAPVMALK TNGDINDLRC
VIKEPHPDPL AACLQQLRKQ SDLQLIRCVR DNARSQRSYL VKPPLLPISL CFKSRQMEHE
FRSKAHRLGS ESELEGGPPT LATPKYNTYI DIFVSFLIYL ATSTSLFLLS PSVYLESYKV
WVCIFMAFST VQLFALFICT KQVCRRTHKY ARRSRPPVTQ SCYDSILSLV SNWYPWHLCG
AVLMSLPVIS ILSNFAMMDV TKFKIFEFHY GFLMFICVIH FCNFTQLNCW MRNTLAFVTS
VAFVGIAIGH MLELKYSAAA ATNNATLIPT PDAPSLQQAQ FDWFHDYRIE IYVDLVLLLV
LVWFLNREFE ISYRLSFYGS AVANQDKIRV QNMKNQADML LHNIIPKYVA EQLKNTAKYS
ENHRNIGIIF ASIVNFNEMY DESYLGGKEY LRVLNELIGD FDELLARPEF RCVEKIKTIG
STFMAASGLD PGSRGEDYEH LYTLLDFAIA MQQVVDSFNR DLLEFNLIMR VGYNFGDVTA
GVIGTSKLYY DIWGDAVNVA SRMDSTGVPG RIQCGLACVP VLSERYDFEP RGKVYVKGKD
HMEVYLLVGK KPDLLGPPEL DVGM
//